(data stored in ACNUC7421 zone)

SWISSPROT: D1CE51_THET1

ID   D1CE51_THET1            Unreviewed;       430 AA.
AC   D1CE51;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375};
DE            EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375};
DE            Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375};
GN   Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375};
GN   OrderedLocusNames=Tter_0285 {ECO:0000313|EMBL:ACZ41207.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41207.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41207.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate = 5-aminolevulinate;
CC         Xref=Rhea:RHEA:14265, ChEBI:CHEBI:57501, ChEBI:CHEBI:356416;
CC         EC=5.4.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_00375,
CC         ECO:0000256|SAAS:SAAS01124572};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00375,
CC         ECO:0000256|SAAS:SAAS01090802};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-
CC       IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090801}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375,
CC       ECO:0000256|SAAS:SAAS01090808}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. HemL subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00375, ECO:0000256|SAAS:SAAS01090804}.
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DR   EMBL; CP001825; ACZ41207.1; -; Genomic_DNA.
DR   RefSeq; WP_012874242.1; NC_013525.1.
DR   STRING; 525904.Tter_0285; -.
DR   EnsemblBacteria; ACZ41207; ACZ41207; Tter_0285.
DR   KEGG; ttr:Tter_0285; -.
DR   eggNOG; ENOG4105CDM; Bacteria.
DR   eggNOG; COG0001; LUCA.
DR   HOGENOM; HOG000020210; -.
DR   KO; K01845; -.
DR   OMA; WGPLIFG; -.
DR   OrthoDB; 493793at2; -.
DR   BioCyc; TTER525904:G1GGS-288-MONOMER; -.
DR   UniPathway; UPA00251; UER00317.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00375; HemL_aminotrans_3; 1.
DR   InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00713; hemL; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CE51.
DR   SWISS-2DPAGE; D1CE51.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090797};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090803};
KW   Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|SAAS:SAAS01090799};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00375,
KW   ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS01090798};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   MOD_RES     269    269       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00375}.
SQ   SEQUENCE   430 AA;  46375 MW;  FD1EC804ED62C02A CRC64;
     MKILANNSSK LFQRAQKVMP GGVSSPVRAF RAVGGEPIFI DKAQGSRLFD VDGKEYIDFV
     GSWGPMILGH AHPEVLRLIH EAVDKGTSFG APNQYELQLA EMVTSLVPSV DVVRFVNSGT
     EATMSAVRLA RAVTSRDLVV KFDGCYHGHA DFFLVAAGSG AMTLGQPDSL GVPNQIASLT
     ASLPYNDIEH VTTFFQERGN EIAAVIVEPV AGNMGVVLPK QDFLAKLREL TSKYGALLIF
     DEVITGFRLS LGGAQQLFDI KPDITTLGKI IGGGLPVGAY GGTAEIMNML APNGPVYQAG
     TLSGNPIAMA AGYKTIHILQ QDEGVYERLD YMGSYLEKGL QDAAKDAGVG VTINRAGSML
     TIFFSSYPVS NYQDAKRSDT TMFAKFHSNM LAQGIYLPPS QFEAWFLSTA HTREDLDRTI
     EAAYTALKKI
//

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